For size exclusion chromatography coupled with multi-angle light scattering (SEC–MALS) analysis, samples (0.2 ml at 1 mg ml−1) were loaded onto a Superdex 200 10/300 GL column (GE Life Sciences, 0.4 ml min−1 in gel filtration buffer) and passed through a Wyatt DAWN Heleos II EOS 18-angle laser photometer coupled to a Wyatt Optilab TrEX differential refractive index detector. Data were analysed using Astra 6 software (Wyatt Technology Corp).
Dawn heleos 2 eos 18 angle laser photometer
Manufactured by Wyatt Technology
The DAWN Heleos II EOS 18-angle laser photometer is a laboratory instrument used to measure the light scattering properties of macromolecules and nanoparticles in solution. It utilizes an 18-angle detection system to provide comprehensive analysis of the size, shape, and molecular weight of these samples.
Automatically generated - may contain errors
Lab products found in correlation
Astra 6, by Wyatt Technology (10 mentions)
Superdex 200 10 300 gl column, by GE Healthcare (6 mentions)
Optilab rex, by Wyatt Technology (2 mentions)
Optilab rex refractive index detector, by Wyatt Technology (2 mentions)
Optilab t rex, by Wyatt Technology (1 mentions)
Superdex 200 10 300 gl, by GE Healthcare (1 mentions)
Superdex 75 10 300 gl, by GE Healthcare (1 mentions)
Qels detector, by Wyatt Technology (1 mentions)
Superdex 200 increase 10 300 gl column, by GE Healthcare (1 mentions)
Superdex 75 10 300 gl column, by GE Healthcare (1 mentions)
13 protocols using dawn heleos 2 eos 18 angle laser photometer
1
SEC-MALS Analysis of Biomolecules
2
SEC-MALS and Analytical Ultracentrifugation of ICP4N Complexes
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Samples of ICP4N·IE3_19mer complexes were prepared as previously described, prior to size exclusion chromatography coupled with multi-angle light scattering (SEC-MALS) analysis. Samples of ICP4N, ICP4NΔIDR and ICP4N·IE3_19mer (0.5 ml at 1 mg/ml) were loaded onto either a Superdex 75 10/300GL or a Superdex 200 10/300GL column (GE life-sciences, 0.75 ml/min in gel filtration buffer) and passed through a Wyatt DAWN Heleos II EOS 18-angle laser photometer coupled to a Wyatt Optilab rEX refractive index detector. Data were analyzed using Astra 6 software (Wyatt Technology Corp.). For sedimentation analytical ultracentrifugation, samples (20 μM protein or 20 μM protein dimer: IE3 1:1 co-purified) were buffer exchanged into 20 mM HEPES, 150 mM NaCl, pH 7.4 by exhaustive dialysis. The sedimentation coefficients for ICP4N in a DNA-free and DNA-bound state were determined from velocity experiments using the Optima XL-I ultracentrifuge (Beckman Instruments) and interference optics. The experiments were performed using double sector cells and sapphire windows and a rotor speed of 48000 rpm, taking 500 scans at 1 min intervals at a temperature of 20°C. The sedimenting boundaries were analyzed using the program Sedfit v8.7.
3
Characterizing Env-NDs via Multi-Angle Light Scattering
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Purified Env-NDs were passed through a Wyatt DAWN Heleos II EOS 18-angle laser photometer coupled to a Wyatt Optilab TrEX differential refractive index detector. Data were analyzed using Astra 6 software (Wyatt Technology Corp).
4
Protein Purification and Characterization
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Tsg samples (0.5 ml at approximately 0.5 mg/ml) were loaded onto a Superdex 200 10/300GL column running at a flow rate of 0.5 ml/min. Proteins eluting from the column passed through a Wyatt DAWN Heleos II EOS 18 angle laser photometer with QELS detector (Wyatt Technologies) and an Optilab T-rEX refractive index detector. The molecular mass and concentrations of the resulting peaks were analysed using ASTRA 5.6.
5
Protein Size Characterization by SEC-MALS
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GpsB samples (500 μl) at concentrations of 8 mg/ml or 0.5 mg/ml were loaded onto a Superdex200 Increase 10/300 GL column (GE Healthcare) equipped with a Jasco UV-2077 detector, Wyatt DAWN Heleos II EOS 18-angle laser photometer (with the 13th detector replaced with the QELS in-line dynamic light scattering detector) coupled to a Wyatt Optilab rEX refractive index detector. The flow rate was 0.75 ml/min. Molecular mass and concentrations of the peaks eluting from the column in a running buffer of 10 mM Tris-HCl pH 8.0, 250 mM NaCl were analyzed using Astra 6.2 (www.wyatt.com/products/software/astra.html ).
6
Multiangle Light Scattering Analysis
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The samples, prepared as described in S1 Text , were passed through a Wyatt DAWN Heleos II EOS 18-angle laser photometer coupled to a Wyatt Optilab TrEX refractive index detector. Data were analyzed with Astra 6 software (Wyatt Technology, Santa Barbara, CA, USA).
7
SEC-MALS Analysis of DENV2 Protein Complexes
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SEC-MALS was performed by loading ∼150 ug of DENV2 FGA02 A259C protein into Superdex 200 10/300 GL column (GE life sciences) and samples were run in Tris 50 mM, NaCl 500 mM (pH 8.0) at a flow rate of 0.4 ml min−1. These samples passed through a Wyatt DAWN Heleos II EOS 18-angle laser photometer coupled to a Wyatt Optilab TrEX differential refractive index detector. Data were later analysed using Astra 6 software (Wyatt Technology Corp).
Analysis of the complex of DENV2 FGA02 WT along with Fab C8 and Fab A11 were performed in similar manner by loading 150 μg of DENV2 FGA02, 300 μg of Fab C8, 300 μg of Fab A11 and for complex formation a mixture of 150 μg of DENV2 FGA02 with 300 μg of FabC8 and 150 μg of DENV2 FGA02 with 300 μg Fab A11. Proteins were injected using 100 μl loop.
Analysis of the complex of DENV2 FGA02 WT along with Fab C8 and Fab A11 were performed in similar manner by loading 150 μg of DENV2 FGA02, 300 μg of Fab C8, 300 μg of Fab A11 and for complex formation a mixture of 150 μg of DENV2 FGA02 with 300 μg of FabC8 and 150 μg of DENV2 FGA02 with 300 μg Fab A11. Proteins were injected using 100 μl loop.
8
Size-Exclusion Chromatography with MALS
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Purified samples of 0.5 ml volume were loaded onto a Superdex75 10/300GL column (GE Healthcare) at 0.75 ml/min in 10 mM Tris pH 7.4, 150 mM NaCl and passed through a Wyatt DAWN Heleos II EOS 18-angle laser photometer coupled to a Wyatt Optilab rEX refractive index detector. Resulting hydrodynamic radii and molecular mass measurements were analysed using Astra 6.
9
Protein Size Analysis by SEC-MALS
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Size exclusion chromatography coupled with multi-angle light scattering (SEC-MALS) analysis was performed at 25 °C. 500 μl of 1.5 mg/ml protein was loaded onto a Superdex 200 10/300GL column (GE Life-Sciences, 0.75 ml/min in 100 mm NaCl, 25 mm Tris/Cl, pH 7.5) and passed through a Wyatt DAWN Heleos II EOS 18-angle laser photometer coupled to a Wyatt O ptilab rEX refractive index detector. Data were analyzed using Astra 6 software (Wyatt Technology Corp.).
10
SEC-MALS and AUC Characterization
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For size exclusion chromatography coupled with multi angle light scattering (SEC-MALS) analysis, samples (0.5 mL at 1 mg/mL) were loaded onto a Superdex 200 10/300GL column (GE life-sciences, 0.75 mL/min in gel filtration buffer) and passed through a Wyatt DAWN Heleos II EOS 18-angle laser photometer coupled to a Wyatt Optilab rEX refractive index detector. Data were analyzed using Astra 6 software (Wyatt Technology Corp., CA, USA). For sedimentation analytical ultracentrifugation, the protein constructs (1 mg/mL) were buffer exchanged into 20 mM HEPES pH 7.4, 150 mM NaCl by exhaustive dialysis. Sedimentation velocity was carried out using a XL-A model centrifuge at 40000 RPM at 20 °C in 450 μL double sector cells. The sedimenting boundary was monitored every 90 seconds using a wavelength of 280 nm for a total of 200 scans. Data were interpreted with the model-based distribution of Lamm equation solutions c(s) using the software Sedfit56 (link). Apparent sedimentation coefficients were obtained by integration of the peak, and the hydrodynamic radius and frictional ratios (f/fo) for the sedimenting dimer were calculated in the program Sednterp57 using the mass obtained from MALS.
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